The human alpha 2-macroglobulin receptor contains high affinity calcium binding sites important for receptor conformation and ligand recognition.
Open Access
- 1 July 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (21) , 12623-12628
- https://doi.org/10.1016/s0021-9258(19)38389-9
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Purification of the human placental α2‐macroglobulin receptorFEBS Letters, 1989
- Characterization, size estimation and solubilization of α-macroglobulin complex receptors in liver membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1989
- Serum and α2‐macroglobulin induce transient hyperpolarizations in the membrane potential of an osteoblastlike cloneJournal of Cellular Physiology, 1987
- Evidence for binding of human pregnancy zone protein-proteinase complex to α2-macroglobulin receptorsBiochimica et Biophysica Acta (BBA) - General Subjects, 1986
- A note on Ca2+ binding to calmodulinBiochemical and Biophysical Research Communications, 1985
- The plasma clearance of human α2-macroglobulin-trypsin complex in the rat is mainly accounted for by uptake into hepatocytesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1985
- Binding of α2-macroglobulin to hepatocytes: Mechanism of in vivo clearanceBiochemical and Biophysical Research Communications, 1985
- Cell association and degradation of α2-macroglobulin-trypsin complexes in hepatocytes and adipocytesBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Continuous cultures of fused cells secreting antibody of predefined specificityNature, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970